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Information on EC 4.2.1.116 - 3-hydroxypropionyl-CoA dehydratase and Organism(s) Metallosphaera sedula and UniProt Accession A4YI89

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.116 3-hydroxypropionyl-CoA dehydratase
IUBMB Comments
Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea . The enzyme from Metallosphaera sedula acts nearly equally as well on (S)-3-hydroxybutanoyl-CoA but not (R)-3-hydroxybutanoyl-CoA .
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Metallosphaera sedula
UNIPROT: A4YI89
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Word Map
The taxonomic range for the selected organisms is: Metallosphaera sedula
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
3-hydroxypropionyl-coa dehydratase, 3hpcd, ms3hpcd, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hydroxypropionyl-coenzyme A dehydratase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-hydroxypropanoyl-CoA = acryloyl-CoA + H2O
show the reaction diagram
molecular mechanism, overview
SYSTEMATIC NAME
IUBMB Comments
3-hydroxypropionyl-CoA hydro-lyase
Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [1]. The enzyme from Metallosphaera sedula acts nearly equally as well on (S)-3-hydroxybutanoyl-CoA but not (R)-3-hydroxybutanoyl-CoA [2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-3-hydroxybutyryl-CoA
crotonyl-CoA + H2O
show the reaction diagram
no substrate: (R)-3-hydroxybutyryl-CoA
-
-
?
3-hydroxypropanoyl-CoA
acryloyl-CoA + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-hydroxypropanoyl-CoA
acryloyl-CoA + H2O
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.075
(S)-3-hydroxybutyryl-CoA
pH 8.6, 65°C
0.0251
3-hydroxypropanoyl-CoA
recombinant enzyme, pH 6.5, 65°C
0.06
3-hydroxypropionyl-CoA
pH 8.6, 65°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
96
3-hydroxypropionyl-CoA
pH 8.6, 65°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
151
purified, recombinant protein, pH 8.6
2.4
extract of autotrophically grown cells, pH 8.6
3.1
extract of heterotrophically grown cells, pH 8.6
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
coupled assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
half-maximal activity
9.5
half-maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
coupled assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
Ms3HPCD shows an overall structure and the CoA-binding mode similar to other enoyl-CoA hydratase (ECH) family enzymes, but compared with the other ECHs, Ms3HPCD has a tightly formed alpha3 helix near the active site, and bulky aromatic residues are located at the enoyl-group binding site, resulting in the enzyme having an optimal substrate binding site for accepting short chain 3-hydroxyacyl-CoA as a substrate. Phylogenetic tree analysis. The 3HPCD homologues from the phylum Crenarchaeota have an enoyl-group binding pocket similar to that of bacterial short-chain ECHs
physiological function
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
220000
recombinant enzyme, gel filtration
23000
gel filtration
28300
1 * 29000, SDS-PAGE, 1 * 28300, calculated
29000
1 * 29000, SDS-PAGE, 1 * 28300, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 28300, about, sequence calculation
homooctamer
8 * 28000, recombinant enzyme, SDS-PAGE
monomer
1 * 29000, SDS-PAGE, 1 * 28300, calculated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme in complex with CoA, hanging drop vapor diffusion method, mixing of 0.001 ml of protein solution containing 41 mg/ml in 40 mM Tris-HCl, pH8.0, with 0.001 ml of reservoir solution, containing consisting of 10% w/v PEG 8000, 0.1 M sodium-potassium phosphate, pH 6.2, 0.2 M NaCl, and 10 mM EDTA, and equilibration against 0.05 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.8 A resolution, modelling
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21 (DE3)-T1 by nickel affinity chromatography and gel filtration to homogeneity
recombinant His-tagged enzyme HPCD from Escherichia coli strain Rosetta 2 (DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene hpcd, recombinant expression of His-tagged enzyme HPCD in Escherichi coli strain Rosetta 2 (DE3), coexpression with 3-hydroxypropionyl-CoA synthetase, acryloyl-CoA reductase, and succinic semialdehyde reductase. Yeast two-hybrid assay for protein interaction analysis of 3-hydroxypropionyl-CoA dehydratase and 3-hydroxypropionyl-CoA synthetase (HPCS-HPCD)
gene Msed_2001, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21 (DE3)-T1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Teufel, R.; Kung, J.; Kockelkorn, D.; Alber, B.; Fuchs, G.
3-Hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales
J. Bacteriol.
191
4572-4581
2009
Metallosphaera sedula (A4YI89), Metallosphaera sedula
Manually annotated by BRENDA team
Loder, A.J.; Han, Y.; Hawkins, A.B.; Lian, H.; Lipscomb, G.L.; Schut, G.J.; Keller, M.W.; Adams, M.W.; Kelly, R.M.
Reaction kinetic analysis of the 3-hydroxypropionate/4-hydroxybutyrate CO2 fixation cycle in extremely thermoacidophilic archaea
Metab. Eng.
38
446-463
2016
Metallosphaera sedula (A4YI89), Metallosphaera sedula, Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2 (A4YI89)
Manually annotated by BRENDA team
Lee, D.; Kim, K.J.
Structural insight into substrate specificity of 3-hydroxypropionyl-coenzyme A dehydratase from Metallosphaera sedula
Sci. Rep.
8
10692
2018
Metallosphaera sedula (A4YI89), Metallosphaera sedula, Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2 (A4YI89)
Manually annotated by BRENDA team